{
  "annotation_id": "9568854b-ae91-4333-9119-4566b27f49f4",
  "date_created": "2026-03-02T18:01:31.673000Z",
  "date_modified": "2026-03-02T18:01:31.673000Z",
  "file_hash": "038a6c5edc881f7e1f06e753996851f7afbc1ccc1fc9ac99a740ffbff3169574",
  "private": false,
  "record": {
    "abstract": "By taking into account base-base stacking interactions we improve the\nGeneralized Model of Polypeptide Chain (GMPC). Based on a one-dimensional\nPotts-like model with many-particle interactions, the GMPC describes the\nhelix-coil transition in both polypeptides and polynucleotides. In the\nframework of the GMPC we show that correctly introduced nearest-neighbor\nstacking interactions against the background of hydrogen bonding lead to\nincreased stability (melting temperature) and, unexpectedly, to decreased\ncooperativity (maximal correlation length). The increase in stability is\nexplained as due to an additional stabilizing interaction (stacking) and the\nsurprising decrease in cooperativity is seen as a result of mixing of\ncontributions of hydrogen bonding and stacking.",
    "arxiv_id": "q-bio/0404014",
    "authors": [
      "Vladimir F. Morozov",
      "Artem V. Badasyan",
      "Arsen V. Grigoryan",
      "Mihran A. Sahakyan",
      "Evgeni Sh. Mamasakhlisov"
    ],
    "categories": [
      "q-bio.BM",
      "q-bio.GN"
    ],
    "doi": "10.1002/bip.20143",
    "journal_ref": "Biopolymers 75, 434 (2004)",
    "title": "Stacking and Hydrogen Bonding. DNA Cooperativity at Melting",
    "url": "https://arxiv.org/abs/q-bio/0404014"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "bf321b49-f65e-45a0-b8d3-2ac75c567536",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}